SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q15149

- PLEC_HUMAN

UniProt

Q15149 - PLEC_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Plectin
Gene
PLEC, PLEC1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofibers integrity.2 Publications

GO - Molecular functioni

  1. ankyrin binding Source: BHF-UCL
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. structural constituent of muscle Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. cell junction assembly Source: Reactome
  3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  4. extracellular matrix organization Source: Reactome
  5. hemidesmosome assembly Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_20537. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Plectin
Short name:
PCN
Short name:
PLTN
Alternative name(s):
Hemidesmosomal protein 1
Short name:
HD1
Plectin-1
Gene namesi
Name:PLEC
Synonyms:PLEC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:9069. PLEC.

Subcellular locationi

Cytoplasmcytoskeleton. Cell junctionhemidesmosome 1 Publication

GO - Cellular componenti

  1. costamere Source: BHF-UCL
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. focal adhesion Source: HPA
  6. hemidesmosome Source: UniProtKB
  7. intermediate filament cytoskeleton Source: HPA
  8. plasma membrane Source: ProtInc
  9. sarcolemma Source: UniProtKB
  10. sarcoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Epidermolysis bullosa simplex with pyloric atresia (EBS-PA) [MIM:612138]: Autosomal recessive genodermatosis characterized by severe skin blistering at birth and congenital pyloric atresia. Death usually occurs in infancy. This disorder is allelic to MD-EBS.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Epidermolysis bullosa simplex, with muscular dystrophy (MD-EBS) [MIM:226670]: A form of epidermolysis bullosa characterized by the association of blister formation at the level of the hemidesmosome with late-onset muscular dystrophy.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti429 – 4291L → LL in MD-EBS. 1 Publication
VAR_011336
Natural varianti1003 – 10053Missing in MD-EBS.
VAR_011337
Epidermolysis bullosa simplex, Ogna type (O-EBS) [MIM:131950]: A form of intraepidermal epidermolysis bullosa characterized by generalized skin bruising, skin fragility with non-scarring blistering and small hemorrhagic blisters on hands. At the ultrastructural level, it is differentiated from classical cases of K-EBS, WC-EBS and DM-EBS, by the occurrence of blisters originating in basal cells above hemidesmosomes, and abnormal hemidesmosome intracellular attachment plates.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2110 – 21101R → W in O-EBS. 1 Publication
VAR_015817
Limb-girdle muscular dystrophy 2Q (LGMD2Q) [MIM:613723]: A form of limb-girdle muscular dystrophy characterized by early childhood onset of proximal muscle weakness. Limb-girdle muscular dystrophies are characterized by proximal weakness, weakness of the hip and shoulder girdles and prominent asymmetrical quadriceps femoris and biceps brachii atrophy.
Note: The disease is caused by mutations affecting the gene represented in this entry. A 9 bp deletion containing the initiation codon in exon 1f of PLEC have been found in limb-girdle muscular dystrophy patients. The mutation results in deficient expression of isoform 9 and disorganization of the myofibers, without any effect on the skin.2 Publications

Keywords - Diseasei

Disease mutation, Epidermolysis bullosa, Limb-girdle muscular dystrophy

Organism-specific databases

MIMi131950. phenotype.
226670. phenotype.
612138. phenotype.
613723. phenotype.
Orphaneti254361. Autosomal recessive limb-girdle muscular dystrophy type 2Q.
257. Epidermolysis bullosa simplex with muscular dystrophy.
158684. Epidermolysis bullosa simplex with pyloric atresia.
79401. Epidermolysis bullosa simplex, Ogna type.
PharmGKBiPA33399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 46844684Plectin
PRO_0000078135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131Phosphothreonine1 Publication
Modified residuei125 – 1251Phosphoserine3 Publications
Modified residuei149 – 1491Phosphoserine3 Publications
Modified residuei720 – 7201Phosphoserine4 Publications
Modified residuei1435 – 14351Phosphoserine4 Publications
Modified residuei1721 – 17211Phosphoserine1 Publication
Modified residuei1725 – 17251N6-acetyllysine By similarity
Modified residuei1732 – 17321Phosphoserine1 Publication
Modified residuei2636 – 26361N6-acetyllysine By similarity
Modified residuei3033 – 30331Phosphotyrosine By similarity
Modified residuei3053 – 30531N6-acetyllysine By similarity
Modified residuei3091 – 30911N6-acetyllysine1 Publication
Modified residuei3362 – 33621Phosphotyrosine By similarity
Modified residuei3420 – 34201N6-acetyllysine1 Publication
Modified residuei4030 – 40301Phosphothreonine4 Publications
Modified residuei4382 – 43821Phosphoserine2 Publications
Modified residuei4384 – 43841Phosphoserine By similarity
Modified residuei4385 – 43851Phosphoserine2 Publications
Modified residuei4386 – 43861Phosphoserine2 Publications
Modified residuei4389 – 43891Phosphoserine2 Publications
Modified residuei4390 – 43901Phosphoserine1 Publication
Modified residuei4391 – 43911Phosphoserine1 Publication
Modified residuei4392 – 43921Phosphoserine1 Publication
Modified residuei4396 – 43961Phosphoserine3 Publications
Modified residuei4400 – 44001Phosphoserine1 Publication
Modified residuei4411 – 44111Phosphothreonine1 Publication
Modified residuei4539 – 45391Phosphothreonine; by CDK1 By similarity
Modified residuei4613 – 46131Phosphoserine3 Publications
Modified residuei4615 – 46151Phosphotyrosine By similarity
Modified residuei4618 – 46181Phosphoserine1 Publication
Modified residuei4622 – 46221Phosphoserine2 Publications
Modified residuei4626 – 46261Phosphoserine3 Publications
Modified residuei4642 – 46421Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated by CDK1; regulates dissociation from intermediate filaments during mitosis By similarity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15149.
PaxDbiQ15149.
PRIDEiQ15149.

PTM databases

PhosphoSiteiQ15149.

Expressioni

Tissue specificityi

Widely expressed with highest levels in muscle, heart, placenta and spinal cord.

Gene expression databases

ArrayExpressiQ15149.
BgeeiQ15149.
CleanExiHS_PLEC1.
GenevestigatoriQ15149.

Organism-specific databases

HPAiCAB003847.
HPA025967.
HPA029906.

Interactioni

Subunit structurei

Homodimer or homotetramer. Interacts (via actin-binding domain) with SYNE3. Interacts (via CH 1 domain) with VIM (via rod region). Interacts (via N-terminus) with DST isoform 2 (via N-terminus). Interacts with FER. Interacts with TOR1A. Interacts with ANK3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FUSP356374EBI-297903,EBI-400434
ITGB4P161447EBI-297903,EBI-948678

Protein-protein interaction databases

BioGridi111355. 55 interactions.
IntActiQ15149. 25 interactions.
MINTiMINT-257064.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi175 – 19319
Helixi194 – 1963
Turni203 – 2097
Helixi211 – 22111
Helixi233 – 24917
Helixi260 – 2634
Helixi267 – 28216
Helixi297 – 30812
Turni309 – 3113
Helixi322 – 3243
Helixi328 – 33710
Helixi339 – 3413
Helixi344 – 3474
Helixi352 – 36716
Helixi375 – 3784
Beta strandi380 – 3823
Helixi385 – 39814
Helixi414 – 44027
Helixi448 – 46417
Helixi466 – 48823
Beta strandi490 – 4923
Helixi500 – 56263
Turni563 – 5664
Helixi572 – 59827
Helixi604 – 62825
Helixi656 – 67823
Helixi685 – 71430
Helixi715 – 7184
Helixi721 – 77858
Helixi788 – 82134
Helixi827 – 85428
Helixi893 – 9008
Helixi904 – 92522
Helixi932 – 9343
Beta strandi944 – 9485
Beta strandi964 – 9707
Beta strandi975 – 9795
Beta strandi985 – 9895
Helixi990 – 9923
Helixi1000 – 102425
Helixi1493 – 152735

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MB8X-ray2.15A175-403[»]
2ODUX-ray2.30A410-640[»]
2ODVX-ray2.05A410-640[»]
3F7PX-ray2.75A/B175-403[»]
3PDYX-ray2.22A/B653-858[»]
3PE0X-ray2.95A/B750-1028[»]
4GDOX-ray1.70A/B/C/D/E/F1492-1530[»]
ProteinModelPortaliQ15149.
SMRiQ15149. Positions 5-101, 175-400, 413-630, 653-1025, 2782-3023, 3441-3681, 4021-4260, 4412-4605.

Miscellaneous databases

EvolutionaryTraceiQ15149.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini175 – 400226Actin-binding
Add
BLAST
Domaini179 – 282104CH 1
Add
BLAST
Domaini295 – 397103CH 2
Add
BLAST
Repeati645 – 71066Spectrin 1
Add
BLAST
Repeati740 – 82485Spectrin 2
Add
BLAST
Repeati837 – 93094Spectrin 3
Add
BLAST
Repeati1315 – 1415101Spectrin 4
Add
BLAST
Repeati2826 – 286338Plectin 1
Add
BLAST
Repeati2864 – 290138Plectin 2
Add
BLAST
Repeati2902 – 293938Plectin 3
Add
BLAST
Repeati2940 – 297738Plectin 4
Add
BLAST
Repeati2981 – 301535Plectin 5
Add
BLAST
Repeati3116 – 315338Plectin 6
Add
BLAST
Repeati3154 – 319138Plectin 7
Add
BLAST
Repeati3192 – 322938Plectin 8
Add
BLAST
Repeati3230 – 326738Plectin 9
Add
BLAST
Repeati3268 – 330538Plectin 10
Add
BLAST
Repeati3306 – 334338Plectin 11
Add
BLAST
Repeati3485 – 352238Plectin 12
Add
BLAST
Repeati3523 – 356038Plectin 13
Add
BLAST
Repeati3561 – 359838Plectin 14
Add
BLAST
Repeati3599 – 363638Plectin 15
Add
BLAST
Repeati3640 – 367435Plectin 16
Add
BLAST
Repeati3820 – 385738Plectin 17
Add
BLAST
Repeati3858 – 389538Plectin 18
Add
BLAST
Repeati3896 – 393338Plectin 19
Add
BLAST
Repeati3934 – 397138Plectin 20
Add
BLAST
Repeati3975 – 400834Plectin 21
Add
BLAST
Repeati4063 – 410038Plectin 22
Add
BLAST
Repeati4101 – 413838Plectin 23
Add
BLAST
Repeati4139 – 417638Plectin 24
Add
BLAST
Repeati4177 – 421438Plectin 25
Add
BLAST
Repeati4218 – 425235Plectin 26
Add
BLAST
Repeati4265 – 430541Plectin 27
Add
BLAST
Repeati4319 – 435638Plectin 28
Add
BLAST
Repeati4408 – 444538Plectin 29
Add
BLAST
Repeati4446 – 448338Plectin 30
Add
BLAST
Repeati4484 – 452138Plectin 31
Add
BLAST
Repeati4522 – 455938Plectin 32
Add
BLAST
Repeati4560 – 459738Plectin 33
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 14701470Globular 1
Add
BLAST
Regioni1471 – 27551285Central fibrous rod domain
Add
BLAST
Regioni2756 – 46841929Globular 2
Add
BLAST
Regioni4250 – 430051Binding to intermediate filaments By similarity
Add
BLAST
Regioni4625 – 4640164 X 4 AA tandem repeats of G-S-R-X
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1469 – 27561288 Reviewed prediction
Add
BLAST

Domaini

The N-terminus interacts with actin, the C-terminus with vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the N- and the C-terminus can bind integrin beta-4.

Sequence similaritiesi

Contains 33 plectin repeats.
Contains 4 spectrin repeats.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5069.
HOVERGENiHBG053616.
InParanoidiQ15149.
KOiK10388.
OMAiYLNKDTH.
PhylomeDBiQ15149.
TreeFamiTF335163.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
3.90.1290.10. 7 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001101. Plectin_repeat.
IPR005326. S10_plectin_N.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF00681. Plectin. 18 hits.
PF03501. S10_plectin. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00250. PLEC. 32 hits.
SM00150. SPEC. 7 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 8 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15149-1) [UniParc]FASTAAdd to Basket

Also known as: Plectin-6

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MVAGMLMPRD QLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR     50
AMASLRARGL VRETFAWCHF YWYLTNEGIA HLRQYLHLPP EIVPASLQRV 100
RRPVAMVMPA RRTPHVQAVQ GPLGSPPKRG PLPTEEQRVY RRKELEEVSP 150
ETPVVPATTQ RTLARPGPEP APATDERDRV QKKTFTKWVN KHLIKAQRHI 200
SDLYEDLRDG HNLISLLEVL SGDSLPREKG RMRFHKLQNV QIALDYLRHR 250
QVKLVNIRND DIADGNPKLT LGLIWTIILH FQISDIQVSG QSEDMTAKEK 300
LLLWSQRMVE GYQGLRCDNF TSSWRDGRLF NAIIHRHKPL LIDMNKVYRQ 350
TNLENLDQAF SVAERDLGVT RLLDPEDVDV PQPDEKSIIT YVSSLYDAMP 400
RVPDVQDGVR ANELQLRWQE YRELVLLLLQ WMRHHTAAFE ERRFPSSFEE 450
IEILWSQFLK FKEMELPAKE ADKNRSKGIY QSLEGAVQAG QLKVPPGYHP 500
LDVEKEWGKL HVAILEREKQ LRSEFERLEC LQRIVTKLQM EAGLCEEQLN 550
QADALLQSDV RLLAAGKVPQ RAGEVERDLD KADSMIRLLF NDVQTLKDGR 600
HPQGEQMYRR VYRLHERLVA IRTEYNLRLK AGVAAPATQV AQVTLQSVQR 650
RPELEDSTLR YLQDLLAWVE ENQHRVDGAE WGVDLPSVEA QLGSHRGLHQ 700
SIEEFRAKIE RARSDEGQLS PATRGAYRDC LGRLDLQYAK LLNSSKARLR 750
SLESLHSFVA AATKELMWLN EKEEEEVGFD WSDRNTNMTA KKESYSALMR 800
ELELKEKKIK ELQNAGDRLL REDHPARPTV ESFQAALQTQ WSWMLQLCCC 850
IEAHLKENAA YFQFFSDVRE AEGQLQKLQE ALRRKYSCDR SATVTRLEDL 900
LQDAQDEKEQ LNEYKGHLSG LAKRAKAVVQ LKPRHPAHPM RGRLPLLAVC 950
DYKQVEVTVH KGDECQLVGP AQPSHWKVLS SSGSEAAVPS VCFLVPPPNQ 1000
EAQEAVTRLE AQHQALVTLW HQLHVDMKSL LAWQSLRRDV QLIRSWSLAT 1050
FRTLKPEEQR QALHSLELHY QAFLRDSQDA GGFGPEDRLM AEREYGSCSH 1100
HYQQLLQSLE QGAQEESRCQ RCISELKDIR LQLEACETRT VHRLRLPLDK 1150
EPARECAQRI AEQQKAQAEV EGLGKGVARL SAEAEKVLAL PEPSPAAPTL 1200
RSELELTLGK LEQVRSLSAI YLEKLKTISL VIRGTQGAEE VLRAHEEQLK 1250
EAQAVPATLP ELEATKASLK KLRAQAEAQQ PTFDALRDEL RGAQEVGERL 1300
QQRHGERDVE VERWRERVAQ LLERWQAVLA QTDVRQRELE QLGRQLRYYR 1350
ESADPLGAWL QDARRRQEQI QAMPLADSQA VREQLRQEQA LLEEIERHGE 1400
KVEECQRFAK QYINAIKDYE LQLVTYKAQL EPVASPAKKP KVQSGSESVI 1450
QEYVDLRTHY SELTTLTSQY IKFISETLRR MEEEERLAEQ QRAEERERLA 1500
EVEAALEKQR QLAEAHAQAK AQAEREAKEL QQRMQEEVVR REEAAVDAQQ 1550
QKRSIQEELQ QLRQSSEAEI QAKARQAEAA ERSRLRIEEE IRVVRLQLEA 1600
TERQRGGAEG ELQALRARAE EAEAQKRQAQ EEAERLRRQV QDESQRKRQA 1650
EVELASRVKA EAEAAREKQR ALQALEELRL QAEEAERRLR QAEVERARQV 1700
QVALETAQRS AEAELQSKRA SFAEKTAQLE RSLQEEHVAV AQLREEAERR 1750
AQQQAEAERA REEAERELER WQLKANEALR LRLQAEEVAQ QKSLAQAEAE 1800
KQKEEAEREA RRRGKAEEQA VRQRELAEQE LEKQRQLAEG TAQQRLAAEQ 1850
ELIRLRAETE QGEQQRQLLE EELARLQREA AAATQKRQEL EAELAKVRAE 1900
MEVLLASKAR AEEESRSTSE KSKQRLEAEA GRFRELAEEA ARLRALAEEA 1950
KRQRQLAEED AARQRAEAER VLAEKLAAIG EATRLKTEAE IALKEKEAEN 2000
ERLRRLAEDE AFQRRRLEEQ AAQHKADIEE RLAQLRKASD SELERQKGLV 2050
EDTLRQRRQV EEEILALKAS FEKAAAGKAE LELELGRIRS NAEDTLRSKE 2100
QAELEAARQR QLAAEEERRR REAEERVQKS LAAEEEAARQ RKAALEEVER 2150
LKAKVEEARR LRERAEQESA RQLQLAQEAA QKRLQAEEKA HAFAVQQKEQ 2200
ELQQTLQQEQ SVLDQLRGEA EAARRAAEEA EEARVQAERE AAQSRRQVEE 2250
AERLKQSAEE QAQARAQAQA AAEKLRKEAE QEAARRAQAE QAALRQKQAA 2300
DAEMEKHKKF AEQTLRQKAQ VEQELTTLRL QLEETDHQKN LLDEELQRLK 2350
AEATEAARQR SQVEEELFSV RVQMEELSKL KARIEAENRA LILRDKDNTQ 2400
RFLQEEAEKM KQVAEEAARL SVAAQEAARL RQLAEEDLAQ QRALAEKMLK 2450
EKMQAVQEAT RLKAEAELLQ QQKELAQEQA RRLQEDKEQM AQQLAEETQG 2500
FQRTLEAERQ RQLEMSAEAE RLKLRVAEMS RAQARAEEDA QRFRKQAEEI 2550
GEKLHRTELA TQEKVTLVQT LEIQRQQSDH DAERLREAIA ELEREKEKLQ 2600
QEAKLLQLKS EEMQTVQQEQ LLQETQALQQ SFLSEKDSLL QRERFIEQEK 2650
AKLEQLFQDE VAKAQQLREE QQRQQQQMEQ ERQRLVASME EARRRQHEAE 2700
EGVRRKQEEL QQLEQQRRQQ EELLAEENQR LREQLQLLEE QHRAALAHSE 2750
EVTASQVAAT KTLPNGRDAL DGPAAEAEPE HSFDGLRRKV SAQRLQEAGI 2800
LSAEELQRLA QGHTTVDELA RREDVRHYLQ GRSSIAGLLL KATNEKLSVY 2850
AALQRQLLSP GTALILLEAQ AASGFLLDPV RNRRLTVNEA VKEGVVGPEL 2900
HHKLLSAERA VTGYKDPYTG QQISLFQAMQ KGLIVREHGI RLLEAQIATG 2950
GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF FDPNTHENLT 3000
YLQLLERCVE DPETGLCLLP LTDKAAKGGE LVYTDSEARD VFEKATVSAP 3050
FGKFQGKTVT IWEIINSEYF TAEQRRDLLR QFRTGRITVE KIIKIIITVV 3100
EEQEQKGRLC FEGLRSLVPA AELLESRVID RELYQQLQRG ERSVRDVAEV 3150
DTVRRALRGA NVIAGVWLEE AGQKLSIYNA LKKDLLPSDM AVALLEAQAG 3200
TGHIIDPATS ARLTVDEAVR AGLVGPEFHE KLLSAEKAVT GYRDPYTGQS 3250
VSLFQALKKG LIPREQGLRL LDAQLSTGGI VDPSKSHRVP LDVACARGCL 3300
DEETSRALSA PRADAKAYSD PSTGEPATYG ELQQRCRPDQ LTGLSLLPLS 3350
EKAARARQEE LYSELQARET FEKTPVEVPV GGFKGRTVTV WELISSEYFT 3400
AEQRQELLRQ FRTGKVTVEK VIKILITIVE EVETLRQERL SFSGLRAPVP 3450
ASELLASGVL SRAQFEQLKD GKTTVKDLSE LGSVRTLLQG SGCLAGIYLE 3500
DTKEKVSIYE AMRRGLLRAT TAALLLEAQA ATGFLVDPVR NQRLYVHEAV 3550
KAGVVGPELH EQLLSAEKAV TGYRDPYSGS TISLFQAMQK GLVLRQHGIR 3600
LLEAQIATGG IIDPVHSHRV PVDVAYQRGY FSEEMNRVLA DPSDDTKGFF 3650
DPNTHENLTY RQLLERCVED PETGLRLLPL KGAEKAEVVE TTQVYTEEET 3700
RRAFEETQID IPGGGSHGGS TMSLWEVMQS DLIPEEQRAQ LMADFQAGRV 3750
TKERMIIIII EIIEKTEIIR QQGLASYDYV RRRLTAEDLF EARIISLETY 3800
NLLREGTRSL REALEAESAW CYLYGTGSVA GVYLPGSRQT LSIYQALKKG 3850
LLSAEVARLL LEAQAATGFL LDPVKGERLT VDEAVRKGLV GPELHDRLLS 3900
AERAVTGYRD PYTEQTISLF QAMKKELIPT EEALRLLDAQ LATGGIVDPR 3950
LGFHLPLEVA YQRGYLNKDT HDQLSEPSEV RSYVDPSTDE RLSYTQLLRR 4000
CRRDDGTGQL LLPLSDARKL TFRGLRKQIT MEELVRSQVM DEATALQLRE 4050
GLTSIEEVTK NLQKFLEGTS CIAGVFVDAT KERLSVYQAM KKGIIRPGTA 4100
FELLEAQAAT GYVIDPIKGL KLTVEEAVRM GIVGPEFKDK LLSAERAVTG 4150
YKDPYSGKLI SLFQAMKKGL ILKDHGIRLL EAQIATGGII DPEESHRLPV 4200
EVAYKRGLFD EEMNEILTDP SDDTKGFFDP NTEENLTYLQ LMERCITDPQ 4250
TGLCLLPLKE KKRERKTSSK SSVRKRRVVI VDPETGKEMS VYEAYRKGLI 4300
DHQTYLELSE QECEWEEITI SSSDGVVKSM IIDRRSGRQY DIDDAIAKNL 4350
IDRSALDQYR AGTLSITEFA DMLSGNAGGF RSRSSSVGSS SSYPISPAVS 4400
RTQLASWSDP TEETGPVAGI LDTETLEKVS ITEAMHRNLV DNITGQRLLE 4450
AQACTGGIID PSTGERFPVT DAVNKGLVDK IMVDRINLAQ KAFCGFEDPR 4500
TKTKMSAAQA LKKGWLYYEA GQRFLEVQYL TGGLIEPDTP GRVPLDEALQ 4550
RGTVDARTAQ KLRDVGAYSK YLTCPKTKLK ISYKDALDRS MVEEGTGLRL 4600
LEAAAQSTKG YYSPYSVSGS GSTAGSRTGS RTGSRAGSRR GSFDATGSGF 4650
SMTFSSSSYS SSGYGRRYAS GSSASLGGPE SAVA 4684
Length:4,684
Mass (Da):531,791
Last modified:October 14, 2008 - v3
Checksum:i04772E4F70A304C8
GO
Isoform 2 (identifier: Q15149-2) [UniParc]FASTAAdd to Basket

Also known as: Plectin-1, 1c

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSGEDAEVRA...PAERAVIRIA

Note: Contains a phosphoserine at position 42.

Show »
Length:4,574
Mass (Da):518,473
Checksum:i7EAEA5A83DEF52EA
GO
Isoform 3 (identifier: Q15149-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSGEDAEVRA...PAERAVIRIA
     409-412: Missing.

Note: Contains a phosphoserine at position 42.

Show »
Length:4,570
Mass (Da):518,032
Checksum:iA0AF260B8C095C8D
GO
Isoform 4 (identifier: Q15149-4) [UniParc]FASTAAdd to Basket

Also known as: Plectin-11, 1a

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSQHQLRVPQ...AVLRASEGKK

Note: Contains a phosphotyrosine at position 26 (By similarity). Contains a phosphoserine at position 21. Contains a phosphoserine at position 20.

Show »
Length:4,547
Mass (Da):516,198
Checksum:i0A1A2AB2E557110A
GO
Isoform 5 (identifier: Q15149-5) [UniParc]FASTAAdd to Basket

Also known as: Plectin-8, 1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.
     138-174: RVYRRKELEEVSPETPVVPATTQRTLARPGPEPAPAT → MEPSGSLFPSLVVVGHVVTLAAVWHWRRGRRWAQDEQ

Show »
Length:4,547
Mass (Da):516,276
Checksum:i0EC98F109B723779
GO
Isoform 6 (identifier: Q15149-6) [UniParc]FASTAAdd to Basket

Also known as: Plectin-10, 1g

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     134-174: TEEQRVYRRK...RPGPEPAPAT → MSGAGGAFAS...GYLYQQLCCV

Show »
Length:4,551
Mass (Da):516,479
Checksum:iC2E0FDA51BC17BF2
GO
Isoform 7 (identifier: Q15149-7) [UniParc]FASTAAdd to Basket

Also known as: Plectin-7, 1d

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: Missing.
     170-174: PAPAT → MKIVP

Show »
Length:4,515
Mass (Da):512,604
Checksum:iC8701AD6D1C1B26E
GO
Isoform 8 (identifier: Q15149-8) [UniParc]FASTAAdd to Basket

Also known as: Plectin-3, 1e

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.
     160-174: QRTLARPGPEPAPAT → MDPSRAIQNEISSLK

Show »
Length:4,525
Mass (Da):513,706
Checksum:i37A4DFAB46C3B4DD
GO
Isoform 9 (identifier: Q15149-9) [UniParc]FASTAAdd to Basket

Also known as: Plectin-2, 1f

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.
     152-174: TPVVPATTQRTLARPGPEPAPAT → MAGPLPDEQDFIQAYEEVREKYK

Show »
Length:4,533
Mass (Da):514,775
Checksum:i5D6382389A66B955
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti429 – 4291L → LL in MD-EBS. 1 Publication
VAR_011336
Natural varianti641 – 6411A → V.
Corresponds to variant rs11136336 [ dbSNP | Ensembl ].
VAR_053585
Natural varianti1003 – 10053Missing in MD-EBS.
VAR_011337
Natural varianti1321 – 13211L → V.1 Publication
Corresponds to variant rs3135109 [ dbSNP | Ensembl ].
VAR_060088
Natural varianti1386 – 13861R → Q.
Corresponds to variant rs11136334 [ dbSNP | Ensembl ].
VAR_060089
Natural varianti1459 – 14591H → R.
Corresponds to variant rs55895668 [ dbSNP | Ensembl ].
VAR_062133
Natural varianti2110 – 21101R → W in O-EBS. 1 Publication
VAR_015817
Natural varianti2150 – 21501R → W.
Corresponds to variant rs34893635 [ dbSNP | Ensembl ].
VAR_053586
Natural varianti2194 – 21941A → V.
Corresponds to variant rs7002002 [ dbSNP | Ensembl ].
VAR_053587
Natural varianti2791 – 27911S → P.
Corresponds to variant rs7833924 [ dbSNP | Ensembl ].
VAR_053588
Natural varianti2821 – 28211R → W.
Corresponds to variant rs35723243 [ dbSNP | Ensembl ].
VAR_053589
Natural varianti2969 – 29691R → H.
Corresponds to variant rs6558407 [ dbSNP | Ensembl ].
VAR_053590
Natural varianti3162 – 31621V → I.
Corresponds to variant rs35027700 [ dbSNP | Ensembl ].
VAR_053591
Natural varianti3171 – 31711A → V.
Corresponds to variant rs35858667 [ dbSNP | Ensembl ].
VAR_053592
Natural varianti3486 – 34861T → M.
Corresponds to variant rs34725742 [ dbSNP | Ensembl ].
VAR_053593
Natural varianti3490 – 34901G → A.
Corresponds to variant rs35261863 [ dbSNP | Ensembl ].
VAR_053594

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 174174MVAGM…PAPAT → MSGEDAEVRAVSEDVSNGSS GSPSPGDTLPWNLGKTQRSR RSGGGAGSNGSVLDPAERAV IRIA in isoform 2 and isoform 3.
VSP_005030Add
BLAST
Alternative sequencei1 – 174174MVAGM…PAPAT → MSQHQLRVPQPEGLGRKRTS SEDNLYLAVLRASEGKK in isoform 4.
VSP_023510Add
BLAST
Alternative sequencei1 – 169169Missing in isoform 7.
VSP_037100Add
BLAST
Alternative sequencei1 – 159159Missing in isoform 8.
VSP_037101Add
BLAST
Alternative sequencei1 – 151151Missing in isoform 9.
VSP_037102Add
BLAST
Alternative sequencei1 – 137137Missing in isoform 5.
VSP_037103Add
BLAST
Alternative sequencei1 – 133133Missing in isoform 6.
VSP_037104Add
BLAST
Alternative sequencei134 – 17441TEEQR…PAPAT → MSGAGGAFASPREVLLERPC WLDGGCEPARRGYLYQQLCC V in isoform 6.
VSP_037105Add
BLAST
Alternative sequencei138 – 17437RVYRR…PAPAT → MEPSGSLFPSLVVVGHVVTL AAVWHWRRGRRWAQDEQ in isoform 5.
VSP_037106Add
BLAST
Alternative sequencei152 – 17423TPVVP…PAPAT → MAGPLPDEQDFIQAYEEVRE KYK in isoform 9.
VSP_037107Add
BLAST
Alternative sequencei160 – 17415QRTLA…PAPAT → MDPSRAIQNEISSLK in isoform 8.
VSP_037108Add
BLAST
Alternative sequencei170 – 1745PAPAT → MKIVP in isoform 7.
VSP_037109
Alternative sequencei409 – 4124Missing in isoform 3.
VSP_005031

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711Y → F in CAA91196. 1 Publication
Sequence conflicti94 – 941P → A in CAA91196. 1 Publication
Sequence conflicti139 – 1391V → L in CAA91196. 1 Publication
Sequence conflicti185 – 1851F → S in CAA91196. 1 Publication
Sequence conflicti259 – 2591N → D in AAB05427. 1 Publication
Sequence conflicti259 – 2591N → D in AAB05428. 1 Publication
Sequence conflicti550 – 5501N → H in CAA91196. 1 Publication
Sequence conflicti560 – 5601V → I in CAA91196. 1 Publication
Sequence conflicti706 – 7061R → Q in CAA91196. 1 Publication
Sequence conflicti886 – 8861Y → N in CAA91196. 1 Publication
Sequence conflicti1002 – 10021A → V in CAA91196. 1 Publication
Sequence conflicti1309 – 13091V → L in AAB05427. 1 Publication
Sequence conflicti1309 – 13091V → L in AAB05428. 1 Publication
Sequence conflicti1334 – 13341V → L in AAB05427. 1 Publication
Sequence conflicti1334 – 13341V → L in AAB05428. 1 Publication
Sequence conflicti1534 – 15341M → I in CAA91196. 1 Publication
Sequence conflicti1662 – 16621A → T in AAB05427. 1 Publication
Sequence conflicti1662 – 16621A → T in AAB05428. 1 Publication
Sequence conflicti1688 – 16903RLR → WLC in CAA91196. 1 Publication
Sequence conflicti1767 – 17671E → Q in CAA91196. 1 Publication
Sequence conflicti1789 – 17891A → L in CAA91196. 1 Publication
Sequence conflicti1910 – 19101R → K in CAA91196. 1 Publication
Sequence conflicti2154 – 21541K → N in AAB05427. 1 Publication
Sequence conflicti2154 – 21541K → N in AAB05428. 1 Publication
Sequence conflicti2154 – 21541K → N in CAA65765. 1 Publication
Sequence conflicti2154 – 21541K → N in AAR95680. 1 Publication
Sequence conflicti2154 – 21541K → N in AAR95682. 1 Publication
Sequence conflicti2154 – 21541K → N in AAR95683. 1 Publication
Sequence conflicti2160 – 21601R → S in CAA91196. 1 Publication
Sequence conflicti2215 – 22151Q → R in CAA91196. 1 Publication
Sequence conflicti2244 – 22441S → A in CAA91196. 1 Publication
Sequence conflicti2244 – 22441S → A in AAB05427. 1 Publication
Sequence conflicti2244 – 22441S → A in AAB05428. 1 Publication
Sequence conflicti2244 – 22441S → A in CAA65765. 1 Publication
Sequence conflicti3027 – 30271K → E in AAB05427. 1 Publication
Sequence conflicti3027 – 30271K → E in AAB05428. 1 Publication
Sequence conflicti3310 – 33101A → E in CAA91196. 1 Publication
Sequence conflicti3361 – 33611L → F in CAA91196. 1 Publication
Sequence conflicti3408 – 34081L → F in CAA91196. 1 Publication
Sequence conflicti3447 – 34471A → S in CAA91196. 1 Publication
Sequence conflicti3531 – 35311A → G in CAA91196. 1 Publication
Sequence conflicti3580 – 35801S → R in CAA91196. 1 Publication
Sequence conflicti3589 – 35891Q → K in CAA91196. 1 Publication
Sequence conflicti3596 – 35961Q → E in CAA91196. 1 Publication
Sequence conflicti3616 – 36161H → N in CAA91196. 1 Publication
Sequence conflicti3686 – 36861A → V in CAA91196. 1 Publication
Sequence conflicti3786 – 37861A → G in CAA91196. 1 Publication
Sequence conflicti3808 – 38081R → K in CAA91196. 1 Publication
Sequence conflicti3816 – 38161A → G in CAA91196. 1 Publication
Sequence conflicti3821 – 38211C → F in CAA91196. 1 Publication
Sequence conflicti3915 – 39151Q → K in CAA91196. 1 Publication
Sequence conflicti3999 – 39991R → K in CAA91196. 1 Publication
Sequence conflicti4007 – 40071T → S in CAA91196. 1 Publication
Sequence conflicti4467 – 44671F → L in CAA91196. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z54367 Genomic DNA. Translation: CAA91196.1.
U53204 mRNA. Translation: AAB05427.1.
U63610, U63609 Genomic DNA. Translation: AAB05428.1.
X97053 mRNA. Translation: CAA65765.1.
AY480044 mRNA. Translation: AAR95677.1.
AY480045 mRNA. Translation: AAR95678.1.
AY480046 mRNA. Translation: AAR95679.1.
AY480047 mRNA. Translation: AAR95680.1.
AY480048 mRNA. Translation: AAR95681.1.
AY480049 mRNA. Translation: AAR95682.1.
AY480050 mRNA. Translation: AAR95683.1.
AY480051 mRNA. Translation: AAR95684.1.
AC109322 Genomic DNA. No translation available.
CCDSiCCDS43769.1. [Q15149-2]
CCDS43770.1. [Q15149-9]
CCDS43771.1. [Q15149-8]
CCDS43772.1. [Q15149-1]
CCDS43773.1. [Q15149-5]
CCDS43774.1. [Q15149-6]
CCDS43775.1. [Q15149-4]
CCDS47936.1. [Q15149-7]
PIRiC59404. A59404.
G02520.
RefSeqiNP_000436.2. NM_000445.4. [Q15149-2]
NP_958780.1. NM_201378.3. [Q15149-9]
NP_958781.1. NM_201379.2. [Q15149-8]
NP_958782.1. NM_201380.3. [Q15149-1]
NP_958783.1. NM_201381.2. [Q15149-7]
NP_958784.1. NM_201382.3. [Q15149-5]
NP_958785.1. NM_201383.2. [Q15149-6]
NP_958786.1. NM_201384.2. [Q15149-4]
UniGeneiHs.434248.

Genome annotation databases

EnsembliENST00000322810; ENSP00000323856; ENSG00000178209. [Q15149-1]
ENST00000345136; ENSP00000344848; ENSG00000178209. [Q15149-4]
ENST00000354589; ENSP00000346602; ENSG00000178209. [Q15149-5]
ENST00000354958; ENSP00000347044; ENSG00000178209. [Q15149-8]
ENST00000356346; ENSP00000348702; ENSG00000178209. [Q15149-9]
ENST00000357649; ENSP00000350277; ENSG00000178209. [Q15149-6]
ENST00000398774; ENSP00000381756; ENSG00000178209. [Q15149-7]
ENST00000436759; ENSP00000388180; ENSG00000178209. [Q15149-2]
ENST00000527096; ENSP00000434583; ENSG00000178209. [Q15149-3]
ENST00000561589; ENSP00000454242; ENSG00000261109. [Q15149-7]
ENST00000561919; ENSP00000455773; ENSG00000261109. [Q15149-8]
ENST00000564962; ENSP00000456105; ENSG00000261109. [Q15149-4]
ENST00000565080; ENSP00000454566; ENSG00000261109. [Q15149-5]
ENST00000565268; ENSP00000455881; ENSG00000261109. [Q15149-2]
ENST00000565557; ENSP00000457504; ENSG00000261109. [Q15149-6]
ENST00000567302; ENSP00000456732; ENSG00000261109. [Q15149-9]
ENST00000568193; ENSP00000455828; ENSG00000261109. [Q15149-1]
ENST00000568204; ENSP00000454559; ENSG00000261109. [Q15149-3]
GeneIDi5339.
KEGGihsa:5339.
UCSCiuc003zab.1. human. [Q15149-4]
uc003zac.1. human. [Q15149-6]
uc003zad.2. human. [Q15149-5]
uc003zae.1. human. [Q15149-7]
uc003zaf.1. human. [Q15149-1]
uc003zag.1. human. [Q15149-8]
uc003zah.2. human. [Q15149-9]
uc003zaj.2. human. [Q15149-2]

Polymorphism databases

DMDMi209572726.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Plectin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z54367 Genomic DNA. Translation: CAA91196.1 .
U53204 mRNA. Translation: AAB05427.1 .
U63610 , U63609 Genomic DNA. Translation: AAB05428.1 .
X97053 mRNA. Translation: CAA65765.1 .
AY480044 mRNA. Translation: AAR95677.1 .
AY480045 mRNA. Translation: AAR95678.1 .
AY480046 mRNA. Translation: AAR95679.1 .
AY480047 mRNA. Translation: AAR95680.1 .
AY480048 mRNA. Translation: AAR95681.1 .
AY480049 mRNA. Translation: AAR95682.1 .
AY480050 mRNA. Translation: AAR95683.1 .
AY480051 mRNA. Translation: AAR95684.1 .
AC109322 Genomic DNA. No translation available.
CCDSi CCDS43769.1. [Q15149-2 ]
CCDS43770.1. [Q15149-9 ]
CCDS43771.1. [Q15149-8 ]
CCDS43772.1. [Q15149-1 ]
CCDS43773.1. [Q15149-5 ]
CCDS43774.1. [Q15149-6 ]
CCDS43775.1. [Q15149-4 ]
CCDS47936.1. [Q15149-7 ]
PIRi C59404. A59404.
G02520.
RefSeqi NP_000436.2. NM_000445.4. [Q15149-2 ]
NP_958780.1. NM_201378.3. [Q15149-9 ]
NP_958781.1. NM_201379.2. [Q15149-8 ]
NP_958782.1. NM_201380.3. [Q15149-1 ]
NP_958783.1. NM_201381.2. [Q15149-7 ]
NP_958784.1. NM_201382.3. [Q15149-5 ]
NP_958785.1. NM_201383.2. [Q15149-6 ]
NP_958786.1. NM_201384.2. [Q15149-4 ]
UniGenei Hs.434248.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MB8 X-ray 2.15 A 175-403 [» ]
2ODU X-ray 2.30 A 410-640 [» ]
2ODV X-ray 2.05 A 410-640 [» ]
3F7P X-ray 2.75 A/B 175-403 [» ]
3PDY X-ray 2.22 A/B 653-858 [» ]
3PE0 X-ray 2.95 A/B 750-1028 [» ]
4GDO X-ray 1.70 A/B/C/D/E/F 1492-1530 [» ]
ProteinModelPortali Q15149.
SMRi Q15149. Positions 5-101, 175-400, 413-630, 653-1025, 2782-3023, 3441-3681, 4021-4260, 4412-4605.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111355. 55 interactions.
IntActi Q15149. 25 interactions.
MINTi MINT-257064.

Chemistry

BindingDBi Q15149.
ChEMBLi CHEMBL1293240.

PTM databases

PhosphoSitei Q15149.

Polymorphism databases

DMDMi 209572726.

Proteomic databases

MaxQBi Q15149.
PaxDbi Q15149.
PRIDEi Q15149.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322810 ; ENSP00000323856 ; ENSG00000178209 . [Q15149-1 ]
ENST00000345136 ; ENSP00000344848 ; ENSG00000178209 . [Q15149-4 ]
ENST00000354589 ; ENSP00000346602 ; ENSG00000178209 . [Q15149-5 ]
ENST00000354958 ; ENSP00000347044 ; ENSG00000178209 . [Q15149-8 ]
ENST00000356346 ; ENSP00000348702 ; ENSG00000178209 . [Q15149-9 ]
ENST00000357649 ; ENSP00000350277 ; ENSG00000178209 . [Q15149-6 ]
ENST00000398774 ; ENSP00000381756 ; ENSG00000178209 . [Q15149-7 ]
ENST00000436759 ; ENSP00000388180 ; ENSG00000178209 . [Q15149-2 ]
ENST00000527096 ; ENSP00000434583 ; ENSG00000178209 . [Q15149-3 ]
ENST00000561589 ; ENSP00000454242 ; ENSG00000261109 . [Q15149-7 ]
ENST00000561919 ; ENSP00000455773 ; ENSG00000261109 . [Q15149-8 ]
ENST00000564962 ; ENSP00000456105 ; ENSG00000261109 . [Q15149-4 ]
ENST00000565080 ; ENSP00000454566 ; ENSG00000261109 . [Q15149-5 ]
ENST00000565268 ; ENSP00000455881 ; ENSG00000261109 . [Q15149-2 ]
ENST00000565557 ; ENSP00000457504 ; ENSG00000261109 . [Q15149-6 ]
ENST00000567302 ; ENSP00000456732 ; ENSG00000261109 . [Q15149-9 ]
ENST00000568193 ; ENSP00000455828 ; ENSG00000261109 . [Q15149-1 ]
ENST00000568204 ; ENSP00000454559 ; ENSG00000261109 . [Q15149-3 ]
GeneIDi 5339.
KEGGi hsa:5339.
UCSCi uc003zab.1. human. [Q15149-4 ]
uc003zac.1. human. [Q15149-6 ]
uc003zad.2. human. [Q15149-5 ]
uc003zae.1. human. [Q15149-7 ]
uc003zaf.1. human. [Q15149-1 ]
uc003zag.1. human. [Q15149-8 ]
uc003zah.2. human. [Q15149-9 ]
uc003zaj.2. human. [Q15149-2 ]

Organism-specific databases

CTDi 5339.
GeneCardsi GC08M144989.
GeneReviewsi PLEC.
H-InvDB HIX0168901.
HGNCi HGNC:9069. PLEC.
HPAi CAB003847.
HPA025967.
HPA029906.
MIMi 131950. phenotype.
226670. phenotype.
601282. gene.
612138. phenotype.
613723. phenotype.
neXtProti NX_Q15149.
Orphaneti 254361. Autosomal recessive limb-girdle muscular dystrophy type 2Q.
257. Epidermolysis bullosa simplex with muscular dystrophy.
158684. Epidermolysis bullosa simplex with pyloric atresia.
79401. Epidermolysis bullosa simplex, Ogna type.
PharmGKBi PA33399.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
HOVERGENi HBG053616.
InParanoidi Q15149.
KOi K10388.
OMAi YLNKDTH.
PhylomeDBi Q15149.
TreeFami TF335163.

Enzyme and pathway databases

Reactomei REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_20537. Type I hemidesmosome assembly.

Miscellaneous databases

ChiTaRSi PLEC. human.
EvolutionaryTracei Q15149.
GeneWikii Plectin.
GenomeRNAii 5339.
NextBioi 20680.
PROi Q15149.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15149.
Bgeei Q15149.
CleanExi HS_PLEC1.
Genevestigatori Q15149.

Family and domain databases

Gene3Di 1.10.418.10. 2 hits.
3.90.1290.10. 7 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001101. Plectin_repeat.
IPR005326. S10_plectin_N.
IPR018159. Spectrin/alpha-actinin.
[Graphical view ]
Pfami PF00307. CH. 2 hits.
PF00681. Plectin. 18 hits.
PF03501. S10_plectin. 1 hit.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00250. PLEC. 32 hits.
SM00150. SPEC. 7 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 8 hits.
PROSITEi PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24)."
    Liu C.-G., Maercker C., Castanon M.J., Hauptmann R., Wiche G.
    Proc. Natl. Acad. Sci. U.S.A. 93:4278-4283(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), DISEASE, VARIANT VAL-1321.
  3. "Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation."
    Zhang T., Haws P., Wu Q.
    Genome Res. 14:79-89(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7; 8 AND 9).
  4. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Tissue: Ovarian carcinoma.
  6. "Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly."
    Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.
    J. Cell Sci. 116:387-399(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH COL17A1, SUBCELLULAR LOCATION.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-1435; SER-1721; THR-4030 AND THR-4411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-4382; SER-4385; SER-4386; SER-4389; SER-4390; SER-4391; SER-4392; SER-4396; SER-4613; SER-4622; SER-4626 AND SER-4642, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
    Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
    J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOR1A.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; THR-4030 AND SER-4626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4386; SER-4389; SER-4396; SER-4613; SER-4618 AND SER-4626, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3091 AND LYS-3420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Mutation in exon 1f of PLEC, leading to disruption of plectin isoform 1f, causes autosomal-recessive limb-girdle muscular dystrophy."
    Gundesli H., Talim B., Korkusuz P., Balci-Hayta B., Cirak S., Akarsu N.A., Topaloglu H., Dincer P.
    Am. J. Hum. Genet. 87:834-841(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF ISOFORM 9, INVOLVEMENT IN LGMD2Q.
  19. "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin."
    Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.
    Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DST.
  20. "Plectin deficiency leads to both muscular dystrophy and pyloric atresia in epidermolysis bullosa simplex."
    Natsuga K., Nishie W., Shinkuma S., Arita K., Nakamura H., Ohyama M., Osaka H., Kambara T., Hirako Y., Shimizu H.
    Hum. Mutat. 31:E1687-E1698(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MD-EBS AND EBS-PA.
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113; SER-125; SER-149; SER-720; SER-1435; SER-1732; THR-4030; SER-4382; SER-4396; SER-4400; SER-4613; SER-4622 AND SER-4642, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-21 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Novel interactions of ankyrins-G at the costameres: the muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C."
    Maiweilidan Y., Klauza I., Kordeli E.
    Exp. Cell Res. 317:724-736(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANK3.
  24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435 AND THR-4030, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain."
    Sonnenberg A., Rojas A.M., de Pereda J.M.
    J. Mol. Biol. 368:1379-1391(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 409-640.
  26. "Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4."
    Garcia-Alvarez B., Bobkov A., Sonnenberg A., de Pereda J.M.
    Structure 11:615-625(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 159-403.
  27. "Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy."
    Pulkkinen L., Smith F.J.D., Shimizu H., Murata S., Yaoita H., Hachisuka H., Nishikawa T., McLean W.H.I., Uitto J.
    Hum. Mol. Genet. 5:1539-1546(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MD-EBS 1003-GLN--ALA-1005 DEL.
  28. "A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency."
    Bauer J.W., Rouan F., Kofler B., Rezniczek G.A., Kornacker I., Muss W., Hametner R., Klausegger A., Huber A., Pohla-Gubo G., Wiche G., Uitto J., Hintner H.
    Am. J. Pathol. 158:617-625(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MD-EBS LEU-429 INS.
  29. "A site-specific plectin mutation causes dominant epidermolysis bullosa simplex Ogna: two identical de novo mutations."
    Koss-Harnes D., Hoeyheim B., Anton-Lamprecht I., Gjesti A., Joergensen R.S., Jahnsen F.L., Olaisen B., Wiche G., Gedde-Dahl T. Jr.
    J. Invest. Dermatol. 118:87-93(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT O-EBS TRP-2110.
  30. "Identification of a lethal form of epidermolysis bullosa simplex associated with a homozygous genetic mutation in plectin."
    Charlesworth A., Gagnoux-Palacios L., Bonduelle M., Ortonne J.-P., De Raeve L., Meneguzzi G.
    J. Invest. Dermatol. 121:1344-1348(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN EBS-PA.

Entry informationi

Entry nameiPLEC_HUMAN
AccessioniPrimary (citable) accession number: Q15149
Secondary accession number(s): Q15148
, Q16640, Q6S376, Q6S377, Q6S378, Q6S379, Q6S380, Q6S381, Q6S382, Q6S383
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 14, 2008
Last modified: September 3, 2014
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi